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9SDP

Cryo-EM structure of the Arabidopsis thaliana 40S ribosomal subunit

This is a non-PDB format compatible entry.
Summary for 9SDP
Entry DOI10.2210/pdb9sdp/pdb
EMDB information54789
Descriptor18S RNA, Small ribosomal subunit protein uS17z, Small ribosomal subunit protein uS15y, ... (23 entities in total)
Functional Keywordsarabidopsis, ribosome, cryoem
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains20
Total formula weight942676.19
Authors
Primary citationKarki, S.,Lu, X.,Paatero, A.O.,Ruonala, R.,Tranter, D.,Guryanov, S.,Rehan, S.,Hellmann, E.,Haakonsson, A.,Butcher, S.J.,Huiskonen, J.T.,Kajander, T.,Helariutta, Y.,Paavilainen, V.O.
Cryo-EM structure of the Arabidopsis thaliana ribosome in translating and non-translating states.
Structure, 34:1195-, 2026
Cited by
PubMed Abstract: Translational control of mRNA expression underpins much of post-transcriptional gene expression driving developmental processes in eukaryotes. How ribosomal mRNA translation is executed in plants may be especially important for adapting to an ever-changing environment. Arabidopsis thaliana is the main genetic model organism in plant science, yet structural insights into developmental processes where ribosomal gene expression plays important roles currently remain lacking. Here, we present cryoelectron microscopy (cryo-EM) structures of the Arabidopsis cytosolic ribosome in both translating and non-translating states, which together provide new structural details into how translation of cytosolic mRNAs is coordinated. Our structures reveal detailed information on the interactions of tRNAs, mRNA, and the nascent polypeptide with subunits of the actively translating 80S ribosome and the role of ribosomal RNA methylation in stabilizing ribosomal subunits. The structures provide a foundation for interpreting the functional effects of many mutations of ribosomal proteins affecting phenotypic effects for plant tissue development.
PubMed: 42361795
DOI: 10.1016/j.str.2026.06.001
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

260626

PDB entries from 2026-10-07

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